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1B23

E. coli cysteinyl-tRNA and T. aquaticus elongation factor EF-TU:GTP ternary complex

Summary for 1B23
Entry DOI10.2210/pdb1b23/pdb
DescriptorCYSTEINYL TRNA, ELONGATION FACTOR TU, MAGNESIUM ION, ... (7 entities in total)
Functional Keywordstranslation elongation factor, transfer rna, protein synthesis, gene regulation-rna complex, gene regulation/rna
Biological sourceEscherichia coli
More
Total number of polymer chains2
Total formula weight69578.83
Authors
Nissen, P.,Kjeldgaard, M.,Thirup, S.,Nyborg, J. (deposition date: 1998-12-04, release date: 1998-12-07, Last modification date: 2023-08-09)
Primary citationNissen, P.,Thirup, S.,Kjeldgaard, M.,Nyborg, J.
The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA.
Structure Fold.Des., 7:143-156, 1999
Cited by
PubMed Abstract: . The translation elongation factor EF-Tu in its GTP-bound state forms a ternary complex with any aminoacylated tRNA (aa-tRNA), except initiator tRNA and selenocysteinyl-tRNA. This complex delivers aa-tRNA to the ribosomal A site during the elongation cycle of translation. The crystal structure of the yeast Phe-tRNAPhe ternary complex with Thermus aquaticus EF-Tu-GDPNP (Phe-TC) has previously been determined as one representative of this general yet highly discriminating complex formation.
PubMed: 10368282
DOI: 10.1016/S0969-2126(99)80021-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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数据于2025-10-08公开中

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